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Search results 401 to 495 out of 495 for Perp

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Type Details Score
Publication
9311808 | -
First Author: Enssle J
Year: 1997
Journal: J Virol
Title: Carboxy-terminal cleavage of the human foamy virus Gag precursor molecule is an essential step in the viral life cycle.
Volume: 71
Issue: 10
Pages: 7312-7
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Protein
Q9DAF3
Organism: Mus musculus/domesticus
Length: 408  
Fragment?: false
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Protein
A2ADY9
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
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Protein
Q9JJR9
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
Q7M732
Organism: Mus musculus/domesticus
Length: 1744  
Fragment?: false
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Protein
B4YB44
Organism: Mus musculus/domesticus
Length: 1744  
Fragment?: false
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Protein
Q6GQT2
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Publication
19173708 | -
 
First Author: Llorens C
Year: 2009
Journal: Biol Direct
Title: Bioinformatic flowchart and database to investigate the origins and diversity of clan AA peptidases.
Volume: 4
Pages: 3
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Publication
25144529 | -
First Author: Cruz R
Year: 2014
Journal: PLoS Pathog
Title: RC1339/APRc from Rickettsia conorii is a novel aspartic protease with properties of retropepsin-like enzymes.
Volume: 10
Issue: 8
Pages: e1004324
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Protein Domain
IPR018061 | Retropepsins
Type: Domain
Description: This group of aspartic peptidases belong to the peptidase clan AA. The clan includes the single domain aspartic proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses) which are active as homodimers. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin [, ]. Family A2 includes the peptidase (retropepsin, EC 3.4.23.16) from the human immunodeficiency virus and other retroviruses. In most retroviruses, the peptidase is encoded as a segment of a polyprotein (usually the pol polyprotein, which includes the peptidase, a reverse transcriptase, RNase H and an integrase, but occassionally the gag polyprotein) which it cleaves during viral maturation to release individual proteins. Some retrotransposon polyproteins also contain a homologous, retropepsin-like peptidase which is also a member of family A2.Family A3 includes peptidases from the double-stranded DNA plant viruses known as badnaviruses or pararetroviruses. The viral genome includes genes (ORFs IV and V) that encodes polyproteins. The ORF V polyprotein contains the peptidase and a reverse transcriptase. The peptidase processes the ORF IV polyprotein, which includes the viral coat protein [].Family A9 includes peptidases from spumaretroviruses, and the peptidase is a component of either the gag and pol polyprotein, which is processes []. The structure has been solved for the peptidase from simian foamy virus and shows a retropepsin-like fold [].Family A11 includes polyprotein-processing peptidases from retrotransposons such as the copia transposon from Drosophila melanogaster. No tertiary structure has been solved for any member of the family, and family A11 is included in clan AA on the basis of the similar motif around the active site Asp.Family A28 includes the yeast DNA-damage inducible protein 1 which is a component of the DNA repair pathway. The tertiary structure shows a retropepsin-like fold []. This peptidase is not a component of a polyprotein.Family A32 includes the bacterial PerP peptidase which converts the transmembrane factor PodJ from a form that recruits proteins for pilus formation, to a truncated form that recruits proteins for stalk formation. This converts the bacterium from a motile form to the sessile form found in biofilms [].Aspartic peptidases, also known as aspartyl proteases ([intenz:3.4.23.-]), are widely distributed proteolytic enzymes [, , ]known to exist in vertebrates, fungi, plants, protozoa, bacteria, archaea, retroviruses and some plant viruses. All known aspartic peptidases are endopeptidases. A water molecule, activated by two aspartic acid residues, acts as the nucleophile in catalysis. Aspartic peptidases can be grouped into five clans, each of which shows a unique structural fold [].Peptidases in clan AA are either bilobed (family A1 or the pepsin family) or are a homodimer (all other families in the clan, including retropepsin from HIV-1/AIDS) []. Each lobe consists of a single domain with a closed β-barrel and each lobe contributes one Asp to form the active site. Most peptidases in the clan are inhibited by the naturally occurring small-molecule inhibitor pepstatin [].Clan AC contains the single family A8: the signal peptidase 2 family. Members of the family are found in all bacteria. Signal peptidase 2 processes the premurein precursor, removing the signal peptide. The peptidase has four transmembrane domains and the active site is on the periplasmic side of the cell membrane. Cleavage occurs on the amino side of a cysteine where the thiol group has been substituted by a diacylglyceryl group. Site-directed mutagenesis has identified two essential aspartic acid residues which occur in the motifs GNXXDRX and FNXAD (where X is a hydrophobic residue) []. No tertiary structures have been solved for any member of the family, but because of the intramembrane location, the structure is assumed not to be pepsin-like.Clan AD contains two families of transmembrane endopeptidases: A22 and A24. These are also known as "GXGD peptidases"because of a common GXGD motif which includes one of the pair of catalytic aspartic acid residues. Structures are known for members of both families and show a unique, common fold with up to nine transmembrane regions []. The active site aspartic acids are located within a large cavity in the membrane into which water can gain access [].Clan AE contains two families, A25 and A31. Tertiary structures have been solved for members of both families and show a common fold consisting of an α-β-alpha sandwich, in which the beta sheet is five stranded [, ].Clan AF contains the single family A26. Members of the clan are membrane-proteins with a unique fold. Homologues are known only from bacteria. The structure of omptin (also known as OmpT) shows a cylindrical barrel containing ten beta strands inserted in the membrane with the active site residues on the outer surface [].There are two families of aspartic peptidases for which neither structure nor active site residues are known and these are not assigned to clans. Family A5 includes thermopsin, an endopeptidase found only in thermophilic archaea. Family A36 contains sporulation factor SpoIIGA, which is known to process and activate sigma factor E, one of the transcription factors that controls sporulation in bacteria [].
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Protein Domain
IPR001995 | Peptidase_A2_cat
Type: Domain
Description: This group of aspartic peptidases belong to the peptidase clan AA. The clan includes the single domain aspartic proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses) which are active as homodimers. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin [, ]. Family A2 includes the peptidase (retropepsin, EC 3.4.23.16) from the human immunodeficiency virus and other retroviruses. In most retroviruses, the peptidase is encoded as a segment of a polyprotein (usually the pol polyprotein, which includes the peptidase, a reverse transcriptase, RNase H and an integrase, but occassionally the gag polyprotein) which it cleaves during viral maturation to release individual proteins. Some retrotransposon polyproteins also contain a homologous, retropepsin-like peptidase which is also a member of family A2.Family A3 includes peptidases from the double-stranded DNA plant viruses known as badnaviruses or pararetroviruses. The viral genome includes genes (ORFs IV and V) that encodes polyproteins. The ORF V polyprotein contains the peptidase and a reverse transcriptase. The peptidase processes the ORF IV polyprotein, which includes the viral coat protein [].Family A9 includes peptidases from spumaretroviruses, and the peptidase is a component of either the gag and pol polyprotein, which is processes []. The structure has been solved for the peptidase from simian foamy virus and shows a retropepsin-like fold [].Family A11 includes polyprotein-processing peptidases from retrotransposons such as the copia transposon from Drosophila melanogaster. No tertiary structure has been solved for any member of the family, and family A11 is included in clan AA on the basis of the similar motif around the active site Asp.Family A28 includes the yeast DNA-damage inducible protein 1 which is a component of the DNA repair pathway. The tertiary structure shows a retropepsin-like fold []. This peptidase is not a component of a polyprotein.Family A32 includes the bacterial PerP peptidase which converts the transmembrane factor PodJ from a form that recruits proteins for pilus formation, to a truncated form that recruits proteins for stalk formation. This converts the bacterium from a motile form to the sessile form found in biofilms [].Aspartic peptidases, also known as aspartyl proteases ([intenz:3.4.23.-]), are widely distributed proteolytic enzymes [, , ]known to exist in vertebrates, fungi, plants, protozoa, bacteria, archaea, retroviruses and some plant viruses. All known aspartic peptidases are endopeptidases. A water molecule, activated by two aspartic acid residues, acts as the nucleophile in catalysis. Aspartic peptidases can be grouped into five clans, each of which shows a unique structural fold [].Peptidases in clan AA are either bilobed (family A1 or the pepsin family) or are a homodimer (all other families in the clan, including retropepsin from HIV-1/AIDS) []. Each lobe consists of a single domain with a closed β-barrel and each lobe contributes one Asp to form the active site. Most peptidases in the clan are inhibited by the naturally occurring small-molecule inhibitor pepstatin [].Clan AC contains the single family A8: the signal peptidase 2 family. Members of the family are found in all bacteria. Signal peptidase 2 processes the premurein precursor, removing the signal peptide. The peptidase has four transmembrane domains and the active site is on the periplasmic side of the cell membrane. Cleavage occurs on the amino side of a cysteine where the thiol group has been substituted by a diacylglyceryl group. Site-directed mutagenesis has identified two essential aspartic acid residues which occur in the motifs GNXXDRX and FNXAD (where X is a hydrophobic residue) []. No tertiary structures have been solved for any member of the family, but because of the intramembrane location, the structure is assumed not to be pepsin-like.Clan AD contains two families of transmembrane endopeptidases: A22 and A24. These are also known as "GXGD peptidases"because of a common GXGD motif which includes one of the pair of catalytic aspartic acid residues. Structures are known for members of both families and show a unique, common fold with up to nine transmembrane regions []. The active site aspartic acids are located within a large cavity in the membrane into which water can gain access [].Clan AE contains two families, A25 and A31. Tertiary structures have been solved for members of both families and show a common fold consisting of an α-β-alpha sandwich, in which the beta sheet is five stranded [, ].Clan AF contains the single family A26. Members of the clan are membrane-proteins with a unique fold. Homologues are known only from bacteria. The structure of omptin (also known as OmpT) shows a cylindrical barrel containing ten beta strands inserted in the membrane with the active site residues on the outer surface [].There are two families of aspartic peptidases for which neither structure nor active site residues are known and these are not assigned to clans. Family A5 includes thermopsin, an endopeptidase found only in thermophilic archaea. Family A36 contains sporulation factor SpoIIGA, which is known to process and activate sigma factor E, one of the transcription factors that controls sporulation in bacteria [].
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Protein
Q09PK2
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
A0A8D3UE05
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: false
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Publication
18597783 | -
First Author: Hartl MJ
Year: 2008
Journal: J Mol Biol
Title: The solution structure of the simian foamy virus protease reveals a monomeric protein.
Volume: 381
Issue: 1
Pages: 141-9
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Protein
Q7TN75
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
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Protein
E9Q3F7
Organism: Mus musculus/domesticus
Length: 1005  
Fragment?: false
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Protein
A0A140LIE6
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Protein
Q05BF3
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: false
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Protein
Q9JIA5
Organism: Mus musculus/domesticus
Length: 341  
Fragment?: true
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Protein
Q7M6U6
Organism: Mus musculus/domesticus
Length: 318  
Fragment?: true
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Protein
Q7TQ38
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: false
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Protein
A0A510NUM0
Organism: Mus musculus/domesticus
Length: 332  
Fragment?: true
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Protein
Q9JIA4
Organism: Mus musculus/domesticus
Length: 318  
Fragment?: true
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Protein
Q3UNK8
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
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Protein
Q3TL09
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
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Protein
Q7M6W4
Organism: Mus musculus/domesticus
Length: 318  
Fragment?: true
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Protein
A0A7G9TMG5
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: false
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Protein
Q61213
Organism: Mus musculus/domesticus
Length: 827  
Fragment?: false
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Protein
F6TV37
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: true
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Protein
Q69ZQ6
Organism: Mus musculus/domesticus
Length: 373  
Fragment?: true
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Protein
Q9CUU5
Organism: Mus musculus/domesticus
Length: 267  
Fragment?: false
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Protein
A0A338P773
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: true
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Protein
D3YZ92
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Protein
V9H0W7
Organism: Mus musculus/domesticus
Length: 1182  
Fragment?: true
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Protein
A0A7S8ZXC7
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
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Protein
Q1KYM2
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
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Protein
P70355
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
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Protein
G4V4Z1
Organism: Mus musculus/domesticus
Length: 1737  
Fragment?: false
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Protein
A0A068ETZ5
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
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Protein
Q1KYL9
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
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Protein
A0A240FAT1
Organism: Mus musculus/domesticus
Length: 1734  
Fragment?: false
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Protein
P56818
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q9D106
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
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Protein
P00796
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
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Protein
P70269
Organism: Mus musculus/domesticus
Length: 397  
Fragment?: false
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Protein
P18242
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q9D7R7
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: false
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Protein
P06281
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Protein
O09043
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q9DCS8
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q91X66
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
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Protein
Q3TXL5
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
F8WIR1
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q3U651
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q8C243
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
A0A1B0GT66
Organism: Mus musculus/domesticus
Length: 273  
Fragment?: true
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Protein
Q3UCW4
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q8VCK2
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
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Protein
Q3U8W5
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q3U7H1
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q3U7I9
Organism: Mus musculus/domesticus
Length: 404  
Fragment?: false
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Protein
Q3TWR6
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q8C7R1
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q3U7P0
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
F6UH57
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
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Protein
F6Y6L6
Organism: Mus musculus/domesticus
Length: 278  
Fragment?: true
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Protein
Q3TIR0
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q3UAQ1
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q3TV11
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: true
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Protein
Q8BQY4
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: false
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Protein
Q3TDT8
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
D3Z6T3
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
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Protein
Q9JM79
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q3TWD0
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q3TWL1
Organism: Mus musculus/domesticus
Length: 335  
Fragment?: true
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Protein
Q3UC89
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q8C4F4
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
B7ZWD6
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
Q3TJN3
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q3UCD9
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
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Protein
Q9JL18
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
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Protein
A0A0R4J0I8
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
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Publication
2194475 | -
 
First Author: Davies DR
Year: 1990
Journal: Annu Rev Biophys Biophys Chem
Title: The structure and function of the aspartic proteinases.
Volume: 19
Pages: 189-215
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Publication
1851433 | -
First Author: Rao JK
Year: 1991
Journal: Biochemistry
Title: Structural and evolutionary relationships between retroviral and eucaryotic aspartic proteinases.
Volume: 30
Issue: 19
Pages: 4663-71
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Publication
6795036 | -
 
First Author: Foltmann B
Year: 1981
Journal: Essays Biochem
Title: Gastric proteinases--structure, function, evolution and mechanism of action.
Volume: 17
Pages: 52-84
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Publication
10331925 | -
First Author: Fritsche E
Year: 1999
Journal: J Mol Biol
Title: Crystal structure of the hydrogenase maturating endopeptidase HYBD from Escherichia coli.
Volume: 288
Issue: 5
Pages: 989-98
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Publication
11566868 | -
First Author: Vandeputte-Rutten L
Year: 2001
Journal: EMBO J
Title: Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.
Volume: 20
Issue: 18
Pages: 5033-9
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Publication
10864493 | -
First Author: Ponnuraj K
Year: 2000
Journal: J Mol Biol
Title: Crystal structure of a novel germination protease from spores of Bacillus megaterium: structural arrangement and zymogen activation.
Volume: 300
Issue: 1
Pages: 1-10
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Publication
2682266 | -
First Author: Lapatto R
Year: 1989
Journal: Nature
Title: X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes.
Volume: 342
Issue: 6247
Pages: 299-302
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Publication
23254940 | -
First Author: Li X
Year: 2013
Journal: Nature
Title: Structure of a presenilin family intramembrane aspartate protease.
Volume: 493
Issue: 7430
Pages: 56-61
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Publication
21765428 | -
First Author: Hu J
Year: 2011
Journal: Nature
Title: The crystal structure of GXGD membrane protease FlaK.
Volume: 475
Issue: 7357
Pages: 528-31
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Publication
4912600 | -
First Author: Umezawa H
Year: 1970
Journal: J Antibiot (Tokyo)
Title: Pepstatin, a new pepsin inhibitor produced by Actinomycetes.
Volume: 23
Issue: 5
Pages: 259-62
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Publication
10497172 | -
First Author: Tjalsma H
Year: 1999
Journal: J Biol Chem
Title: The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis.
Volume: 274
Issue: 40
Pages: 28191-7
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Publication
21751400 | -
First Author: Junne S
Year: 2011
Journal: Biotechnol J
Title: A two-compartment bioreactor system made of commercial parts for bioprocess scale-down studies: impact of oscillations on Bacillus subtilis fed-batch cultivations.
Volume: 6
Issue: 8
Pages: 1009-17
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Publication
8439290 | -
 
First Author: Rawlings ND
Year: 1993
Journal: Biochem J
Title: Evolutionary families of peptidases.
Volume: 290 ( Pt 1)
Pages: 205-18
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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